ID   RACYT_RANTE             Reviewed;          62 AA.
AC   P83719;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Ranacyclin-T;
DE   Flags: Precursor;
GN   Name=RNCT;
OS   Rana temporaria (European common frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=8407 {ECO:0000312|EMBL:CAE48162.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT LYS-60, SYNTHESIS, FUNCTION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Skin {ECO:0000312|EMBL:CAE48162.1};
RX   PubMed=14636071; DOI=10.1021/bi034521l;
RA   Mangoni M.L., Papo N., Mignogna G., Andreu D., Shai Y., Barra D.,
RA   Simmaco M.;
RT   "Ranacyclins, a new family of short cyclic antimicrobial peptides:
RT   biological function, mode of action and parameters involved in target
RT   specificity.";
RL   Biochemistry 42:14023-14035(2003).
CC   -!- FUNCTION: Has antibacterial activity against Gram-positive bacteria
CC       B.megaterium Bm11, S.lentus and M.luteus, and Gram-negative bacteria
CC       E.coli D22, Y.pseudotuberculosis YP III and P.syringae pv tabaci, and
CC       antifungal activity against C.albicans ATCC 10231, C.tropicalis,
CC       C.guiller-mondii and P.nicotianae spores. Has weak hemolytic activity.
CC       The mature peptide inserts into the hydrophobic core of the bacterial
CC       cell membrane and increases permeability without disrupting membrane
CC       integrity. Probably binds to the outer membrane surface before
CC       aggregating to form transmembrane pores. {ECO:0000269|PubMed:14636071,
CC       ECO:0000303|PubMed:14636071}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83663}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin granular glands.
CC       {ECO:0000269|PubMed:14636071}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   EMBL; AJ583866; CAE48162.1; -; mRNA.
DR   AlphaFoldDB; P83719; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR032019; Frog_antimicrobial_Ranidae.
DR   Pfam; PF16048; Antimicrobial23; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Disulfide bond; Fungicide;
KW   Hemolysis; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..43
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003463"
FT   PEPTIDE         44..60
FT                   /note="Ranacyclin-T"
FT                   /id="PRO_0000003464"
FT   MOD_RES         60
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:14636071"
FT   DISULFID        49..59
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   62 AA;  6983 MW;  55A4283837A11E82 CRC64;
     MFTMKKTLLV LFFLGVVSLS LCVEERDADE EDGGEVMEEE VKRGALRGCW TKSYPPKPCK
     GK